Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 105, Issue 47, Pages 18145-18152Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0807005105
Keywords
electrospray ionization; gaseous proteins; mass spectrometry; protein conformations; proteomics
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Funding
- Austrian Fonds zur Forderung der wissenschaftlichen Forschung [V59, Y372]
- U.S. National Institute of General Medical Sciences
- National Institutes of Health [GM 16609]
- Austrian Science Fund (FWF) [V59] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [Y 372] Funding Source: researchfish
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Mass spectrometry (MS) has been revolutionized by electrospray ionization (ESI), which is sufficiently gentle to introduce nonvolatile biomolecules such as proteins and nucleic acids (RNA or DNA) into the gas phase without breaking covalent bonds. Although in some cases noncovalent bonding can be maintained sufficiently for ESI/MS characterization of the solution structure of large protein complexes and native enzyme/substrate binding, the new gaseous environment can ultimately cause dramatic structural alterations. The temporal (picoseconds to minutes) evolution of native protein structure during and after transfer into the gas phase, as proposed here based on a variety of studies, can involve side-chain collapse, unfolding, and refolding into new, non-native structures. Control of individual experimental factors allows optimization for specific research objectives.
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